2b5d: Difference between revisions

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<StructureSection load='2b5d' size='340' side='right'caption='[[2b5d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
<StructureSection load='2b5d' size='340' side='right'caption='[[2b5d]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[2b5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thema Thema]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5D FirstGlance]. <br>
<table><tr><td colspan='2'>[[2b5d]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Thermotoga_maritima_MSB8 Thermotoga maritima MSB8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2B5D OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2B5D FirstGlance]. <br>
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1ufa|1ufa]]</div></td></tr>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">tm1438 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243274 THEMA])</td></tr>
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[https://en.wikipedia.org/wiki/Alpha-amylase Alpha-amylase], with EC number [https://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.2.1.1 3.2.1.1] </span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5d OCA], [https://pdbe.org/2b5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5d RCSB], [https://www.ebi.ac.uk/pdbsum/2b5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5d ProSAT]</span></td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2b5d FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2b5d OCA], [https://pdbe.org/2b5d PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2b5d RCSB], [https://www.ebi.ac.uk/pdbsum/2b5d PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2b5d ProSAT]</span></td></tr>
</table>
</table>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b5d ConSurf].
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2b5d ConSurf].
<div style="clear:both"></div>
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
alpha-Amylases are essential enzymes in alpha-glucan metabolism and catalyse the hydrolysis of long sugar polymers such as amylose and starch. The crystal structure of a previously unidentified amylase (AmyC) from the hyperthermophilic organism Thermotoga maritima was determined at 2.2 Angstroms resolution by means of MAD. AmyC lacks sequence similarity to canonical alpha-amylases, which belong to glycosyl hydrolase families 13, 70 and 77, but exhibits significant similarity to a group of as yet uncharacterized proteins in COG1543 and is related to glycerol hydrolase family 57 (GH-57). AmyC reveals features that are characteristic of alpha-amylases, such as a distorted TIM-barrel structure formed by seven beta-strands and alpha-helices (domain A), and two additional but less well conserved domains. The latter are domain B, which contains three helices inserted in the TIM-barrel after beta-sheet 2, and domain C, a five-helix region at the C-terminus. Interestingly, despite moderate sequence homology, structure comparison revealed significant similarities to a member of GH-57 with known three-dimensional structure, Thermococcus litoralis 4-glucanotransferase, and an even higher similarity to a structure of an enzyme of unknown function from Thermus thermophilus.
Structure of the novel alpha-amylase AmyC from Thermotoga maritima.,Dickmanns A, Ballschmiter M, Liebl W, Ficner R Acta Crystallogr D Biol Crystallogr. 2006 Mar;62(Pt 3):262-70. Epub 2006, Feb 22. PMID:16510973<ref>PMID:16510973</ref>
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2b5d" style="background-color:#fffaf0;"></div>


==See Also==
==See Also==
*[[Amylase 3D structures|Amylase 3D structures]]
*[[Amylase 3D structures|Amylase 3D structures]]
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Alpha-amylase]]
[[Category: Large Structures]]
[[Category: Large Structures]]
[[Category: Thema]]
[[Category: Thermotoga maritima MSB8]]
[[Category: Ballschmiter, M]]
[[Category: Ballschmiter M]]
[[Category: Dickmanns, A]]
[[Category: Dickmanns A]]
[[Category: Ficner, R]]
[[Category: Ficner R]]
[[Category: Liebl, W]]
[[Category: Liebl W]]
[[Category: Hydrolase]]

Latest revision as of 16:42, 13 March 2024

Crystal structure of the novel alpha-amylase AmyC from Thermotoga maritimaCrystal structure of the novel alpha-amylase AmyC from Thermotoga maritima

Structural highlights

2b5d is a 1 chain structure with sequence from Thermotoga maritima MSB8. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 2.2Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

See Also

2b5d, resolution 2.20Å

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OCA
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